5d68 - Revision history

OCA at 08:43, 27 September 2023

2023-09-27T08:43:40Z

←Older revision		Revision as of 08:43, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D68 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D68 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [https://pdbe.org/5d68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [https://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.908Å</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [https://pdbe.org/5d68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [https://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 10:23, 21 June 2023

2023-06-21T10:23:20Z

←Older revision		Revision as of 10:23, 21 June 2023
Line 3:		Line 3:
	<StructureSection load='5d68' size='340' side='right'caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>		<StructureSection load='5d68' size='340' side='right'caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5D68 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D68 FirstGlance]. <br>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KRIT1, CCM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [https://pdbe.org/5d68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [https://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [~~http~~://pdbe.org/5d68 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Hereditary cerebral cavernous malformation. Cerebral cavernous malformations 1 (CCM1) [MIM:[~~http~~://omim.org/entry/116860 116860]]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:12172908</ref>	+	[https://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN] Hereditary cerebral cavernous malformation. Cerebral cavernous malformations 1 (CCM1) [MIM:[https://omim.org/entry/116860 116860]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:12172908</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits EKR1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.<ref>PMID:20332120</ref> <ref>PMID:20668652</ref> <ref>PMID:20616044</ref> <ref>PMID:21633110</ref> [REFERENCE:17]	+	[https://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits EKR1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.<ref>PMID:20332120</ref> <ref>PMID:20668652</ref> <ref>PMID:20616044</ref> <ref>PMID:21633110</ref> [REFERENCE:17]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Boggon~~, T J~~]]	+	[[Category: Boggon TJ]]
-	[[Category: Li, X]]	+	[[Category: Li X]]
-	[[Category: Zhang, R]]	+	[[Category: Zhang R]]
-	~~[[Category: Ankyrin repeat domain]]~~	+
-	~~[[Category: Cerebral cavernous malformation]]~~	+
-	~~[[Category: Ferm domain]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 08:47, 18 December 2019

2019-12-18T08:47:42Z

←Older revision		Revision as of 08:47, 18 December 2019
Line 1:		Line 1:

	==Crystal structure of KRIT1 ARD-FERM==		==Crystal structure of KRIT1 ARD-FERM==
-	<StructureSection load='5d68' size='340' side='right' caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>	+	<StructureSection load='5d68' size='340' side='right'caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D68 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D68 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [http://pdbe.org/5d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [http://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KRIT1, CCM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [http://pdbe.org/5d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [http://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Boggon, T J]]		[[Category: Boggon, T J]]
	[[Category: Li, X]]		[[Category: Li, X]]

OCA at 06:38, 6 October 2017

2017-10-06T06:38:11Z

←Older revision		Revision as of 06:38, 6 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of KRIT1 ARD-FERM==		==Crystal structure of KRIT1 ARD-FERM==
	<StructureSection load='5d68' size='340' side='right' caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>		<StructureSection load='5d68' size='340' side='right' caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D68 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D68 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [http://pdbe.org/5d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [http://www.ebi.ac.uk/pdbsum/5d68 PDBsum]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [http://pdbe.org/5d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [http://www.ebi.ac.uk/pdbsum/5d68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d68 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 20:15, 30 November 2015

2015-11-30T20:15:35Z

←Older revision		Revision as of 20:15, 30 November 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits EKR1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.<ref>PMID:20332120</ref> <ref>PMID:20668652</ref> <ref>PMID:20616044</ref> <ref>PMID:21633110</ref> [REFERENCE:17]		[[http://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits EKR1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.<ref>PMID:20332120</ref> <ref>PMID:20668652</ref> <ref>PMID:20616044</ref> <ref>PMID:21633110</ref> [REFERENCE:17]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cerebral cavernous malformations (CCM) are vascular dysplasias that usually occur in the brain and are associated with mutations in the KRIT1/CCM1, CCM2/MGC4607/OSM/Malcavernin, and PDCD10/CCM3/TFAR15 genes. Here we report the 2.9A crystal structure of the ankyrin repeat domain (ARD) and FERM domain of the protein product of KRIT1 (KRIT1; Krev interaction trapped 1). The crystal structure reveals that the KRIT1 ARD contains 4 ankyrin repeats. There is an unusual conformation in the ANK4 repeat that is stabilized by Trp-404, and the structure reveals a solvent exposed ankyrin groove. Domain orientations of the three copies within the asymmetric unit suggest a stable interaction between KRIT1 ARD and FERM domains, indicating a globular ARD-FERM module. This resembles the additional F0 domain found N-terminal to the FERM domain of talin. Structural analysis of KRIT1 ARD-FERM highlights surface regions of high evolutionary conservation, and suggests potential sites that could mediate interaction with binding partners. The structure therefore provides a better understanding of KRIT1 at the molecular level.
		+
		+	Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface.,Zhang R, Li X, Boggon TJ J Struct Biol. 2015 Dec;192(3):449-56. doi: 10.1016/j.jsb.2015.10.006. Epub 2015 , Oct 14. PMID:26458359<ref>PMID:26458359</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5d68" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:33, 22 October 2015

2015-10-22T05:33:45Z

←Older revision		Revision as of 05:33, 22 October 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of KRIT1 ARD-FERM==
-		+	<StructureSection load='5d68' size='340' side='right' caption='[[5d68]], [[Resolution\|resolution]] 2.91Å' scene=''>
-	~~The entry~~ 5d68 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5d68]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D68 FirstGlance]. <br>
-	~~Authors~~: ~~Zhang~~, R., Li, X., ~~Boggon, T~~.J.	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d68 OCA], [http://pdbe.org/5d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d68 RCSB], [http://www.ebi.ac.uk/pdbsum/5d68 PDBsum]</span></td></tr>
-		+	</table>
-	~~Description~~:	+	== Disease ==
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	[[http://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Hereditary cerebral cavernous malformation. Cerebral cavernous malformations 1 (CCM1) [MIM:[http://omim.org/entry/116860 116860]]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:12172908</ref>
-	[[Category: Boggon, T.J]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KRIT1_HUMAN KRIT1_HUMAN]] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits EKR1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.<ref>PMID:20332120</ref> <ref>PMID:20668652</ref> <ref>PMID:20616044</ref> <ref>PMID:21633110</ref> [REFERENCE:17]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Boggon, T J]]
	[[Category: Li, X]]		[[Category: Li, X]]
	[[Category: Zhang, R]]		[[Category: Zhang, R]]
		+	[[Category: Ankyrin repeat domain]]
		+	[[Category: Cerebral cavernous malformation]]
		+	[[Category: Ferm domain]]
		+	[[Category: Signaling protein]]

OCA: Protected "5d68" [edit=sysop:move=sysop]

2015-08-20T11:25:37Z

Protected "5d68" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:25, 20 August 2015

OCA: New page: '''Unreleased structure''' The entry 5d68 is ON HOLD until Paper Publication Authors: Zhang, R., Li, X., Boggon, T.J. Description: Category: Unreleased Structures [[Category: Bogg...

2015-08-20T11:25:35Z

New page: '''Unreleased structure''' The entry 5d68 is ON HOLD until Paper Publication Authors: Zhang, R., Li, X., Boggon, T.J. Description: Category: Unreleased Structures [[Category: Bogg...

New page

'''Unreleased structure'''

The entry 5d68 is ON HOLD until Paper Publication

Authors: Zhang, R., Li, X., Boggon, T.J.

Description:
[[Category: Unreleased Structures]]
[[Category: Boggon, T.J]]
[[Category: Li, X]]
[[Category: Zhang, R]]